Wesolowski P, Wales D, Pracht P
J Phys Chem B. 2024; 128(13):3145-3156.
PMID: 38512062
PMC: 11000224.
DOI: 10.1021/acs.jpcb.4c00104.
Sakata N, Murakami Y, Miyazawa M, Shimamoto S, Hidaka Y
Molecules. 2023; 28(8).
PMID: 37110728
PMC: 10142513.
DOI: 10.3390/molecules28083494.
Narayan M
Molecules. 2020; 25(22).
PMID: 33207635
PMC: 7697891.
DOI: 10.3390/molecules25225337.
Sohail A, Gaikwad M, Khadka P, Saaranen M, Ruddock L
Int J Mol Sci. 2020; 21(3).
PMID: 31973001
PMC: 7037224.
DOI: 10.3390/ijms21030688.
Esperante S, Covaleda G, Trejo S, Bronsoms S, Aviles F, Ventura S
Sci Rep. 2017; 7(1):5457.
PMID: 28710462
PMC: 5511257.
DOI: 10.1038/s41598-017-05657-7.
Protein folding guides disulfide bond formation.
Qin M, Wang W, Thirumalai D
Proc Natl Acad Sci U S A. 2015; 112(36):11241-6.
PMID: 26297249
PMC: 4568676.
DOI: 10.1073/pnas.1503909112.
High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli.
Nozach H, Fruchart-Gaillard C, Fenaille F, Beau F, Ramos O, Douzi B
Microb Cell Fact. 2013; 12:37.
PMID: 23607455
PMC: 3668227.
DOI: 10.1186/1475-2859-12-37.
Direct observation of disulfide isomerization in a single protein.
Alegre-Cebollada J, Kosuri P, Rivas-Pardo J, Fernandez J
Nat Chem. 2011; 3(11):882-7.
PMID: 22024885
PMC: 3205468.
DOI: 10.1038/nchem.1155.
Application of proteases to the identification of chiral modifications in synthetic peptides.
Keating K
J Biomol Tech. 2009; 10(2):72-81.
PMID: 19499010
PMC: 2291589.
Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.
Fei L, Perrett S
J Biol Chem. 2009; 284(17):11134-41.
PMID: 19258323
PMC: 2670118.
DOI: 10.1074/jbc.M809673200.
Conformational isomers of denatured and unfolded proteins: methods of production and applications.
Chang J
Protein J. 2009; 28(1):44-56.
PMID: 19184383
DOI: 10.1007/s10930-009-9162-7.
Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from tarantulas.
Yuan C, He Q, Peng K, Diao J, Jiang L, Tang X
PLoS One. 2008; 3(10):e3414.
PMID: 18923708
PMC: 2561067.
DOI: 10.1371/journal.pone.0003414.
Denaturation and unfolding of human anaphylatoxin C3a: an unusually low covalent stability of its native disulfide bonds.
Chang J, Lin C, Salamanca S, Pangburn M, Wetsel R
Arch Biochem Biophys. 2008; 480(2):104-10.
PMID: 18854167
PMC: 2636726.
DOI: 10.1016/j.abb.2008.09.013.
The autodisplay story, from discovery to biotechnical and biomedical applications.
Jose J, Meyer T
Microbiol Mol Biol Rev. 2007; 71(4):600-19.
PMID: 18063719
PMC: 2168652.
DOI: 10.1128/MMBR.00011-07.
Pathway of oxidative folding of a 3-disulfide alpha-lactalbumin may resemble either BPTI model or hirudin model.
Salamanca S, Chang J
Protein J. 2006; 25(4):275-87.
PMID: 16710754
DOI: 10.1007/s10930-006-9011-x.
Oxidative folding of hirudin in human serum.
Chang J, Lu B, Lai P
Biochem J. 2005; 394(Pt 1):249-57.
PMID: 16271042
PMC: 1386023.
DOI: 10.1042/BJ20051660.
Graph-representation of oxidative folding pathways.
Agoston V, Cemazar M, Kajan L, Pongor S
BMC Bioinformatics. 2005; 6:19.
PMID: 15676070
PMC: 549202.
DOI: 10.1186/1471-2105-6-19.
Structure and heterogeneity of the one- and two-disulfide folding intermediates of tick anticoagulant peptide.
Chang J, Ballatore A
J Protein Chem. 2000; 19(4):299-310.
PMID: 11043935
DOI: 10.1023/a:1007099430211.
On the thermal unfolding character of globular proteins.
Muthusamy R, Gromiha M, Ponnuswamy P
J Protein Chem. 2000; 19(1):1-8.
PMID: 10882167
DOI: 10.1023/a:1007027623966.
Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry.
Wu J, Yang Y, Watson J
Protein Sci. 1998; 7(4):1017-28.
PMID: 9568908
PMC: 2143974.
DOI: 10.1002/pro.5560070419.